BACKGROUND: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. RESULTS: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. CONCLUSIONS: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.
BACKGROUND: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. RESULTS: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. CONCLUSIONS: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.
Authors: Je-Hyun Yoon; Supriyo De; Subramanya Srikantan; Kotb Abdelmohsen; Ioannis Grammatikakis; Jiyoung Kim; Kyoung Mi Kim; Ji Heon Noh; Elizabeth J F White; Jennifer L Martindale; Xiaoling Yang; Min-Ju Kang; William H Wood; Nicole Noren Hooten; Michele K Evans; Kevin G Becker; Vidisha Tripathi; Kannanganattu V Prasanth; Gerald M Wilson; Thomas Tuschl; Nicholas T Ingolia; Markus Hafner; Myriam Gorospe Journal: Nat Commun Date: 2014-11-04 Impact factor: 14.919
Authors: Jens Eilbracht; Michaela Reichenzeller; Michaela Hergt; Martina Schnölzer; Hans Heid; Michael Stöhr; Werner W Franke; Marion S Schmidt-Zachmann Journal: Mol Biol Cell Date: 2004-01-23 Impact factor: 4.138
Authors: Xiangting Wang; Xiaoyuan Song; Christopher K Glass; Michael G Rosenfeld Journal: Cold Spring Harb Perspect Biol Date: 2011-01-01 Impact factor: 10.005
Authors: Guadalupe Sabio; María I Cerezo-Guisado; Paloma Del Reino; Francisco A Iñesta-Vaquera; Simon Rousseau; J Simon C Arthur; David G Campbell; Francisco Centeno; Ana Cuenda Journal: J Cell Sci Date: 2010-07-06 Impact factor: 5.285